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PubMed · 6874424

Simultaneous azo-coupling method for an estrogen sulfatase in human tissues.

S Partanen
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Abstract

A simultaneous azo-coupling method for the histochemical localization of d-equilenin sulfatase is described. d-Equilenin is a natural estrogenic steroid hormone, and its sulfuric acid ester was synthesized. It was found that the d-equilenin liberated during hydrolysis of d-equilenin sulfate by tissue sulfatase could be coupled with a diazonium salt to produce a purple precipitate indicating enzyme activity. d-Equilenin sulfatase was found in human tissues, but not in tissues of the rat. The optimum substrate concentration was 0.8 mM, activity was demonstrable over the wide pH range 5.0-8.0. Enzyme activity localized diffusely in the cytoplasm in optimally fixed specimens. Enzyme activity was also fairly well demonstrable in unfixed cryostat sections. Enzyme activity was completely inhibited by 0.1 M phosphate, 1 mM sodium tetraborate, 1 mM p-nitrophenyl sulfate and by 2 mM p-nitrocatechol sulfate. Estrone sulfate at concentration 0.8 mM had no effect, but at 4 mM caused marked inhibition of the reaction. At the same concentrations dehydroepiandrosterone sulfate did not inhibit the reaction. The chemical properties and tissue localizations of d-equilenin sulfatase differed from the properties of arylsulfatases A, B and C and other steroid sulfatases reported previously in the literature.

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17-KetosteroidsAdrenal MedullaBreastDiazonium CompoundsEndometriumEquileninFemaleHistocytochemistryHumansHydrogen-Ion ConcentrationKidney TubulesMaleOvaryPregnancyRosaniline DyesSkinSulfatasesTime FactorsToluidinesTrophoblastsJournal Article

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S Partanen. 1983. Simultaneous azo-coupling method for an estrogen sulfatase in human tissues.. https://doi.org/10.1007/bf00489502

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